Reviewed, UniProtKB/Swiss-Prot Q27772 (C1TC_SPOFR)

Names and origin

Protein names	Recommended name:     C-1-tetrahydrofolate synthase, cytoplasmic       Short name=C1-THF synthase Including the following 3 domains:     1- Recommended name:             Methylenetetrahydrofolate dehydrogenase               EC=1.5.1.5     2- Recommended name:             Methenyltetrahydrofolate cyclohydrolase               EC=3.5.4.9     3- Recommended name:             Formyltetrahydrofolate synthetase               EC=6.3.4.3
Organism	Spodoptera frugiperda (Fall armyworm)
Taxonomic identifier	7108 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Noctuoidea › Noctuidae › Amphipyrinae › Spodoptera

Protein attributes

Sequence length	933 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.
Pathway	One-carbon metabolism; tetrahydrofolate pathway.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.
Sequence similarities	In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family. In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis Methionine biosynthesis One-carbon metabolism Purine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Hydrolase Ligase Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW formate-tetrahydrofolate ligase activity Inferred from electronic annotation. Source: EC methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: EC methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 933	933	C-1-tetrahydrofolate synthase, cytoplasmic		PRO_0000199325
Regions
	Nucleotide binding	170 – 172	3	NADP By similarity
	Nucleotide binding	378 – 385	8	ATP By similarity
	Region	1 – 303	303	Methylenetetrahydrofolate dehydrogenase and cyclohydrolase
	Region	51 – 55	5	Substrate binding By similarity
	Region	98 – 100	3	Substrate binding By similarity
	Region	270 – 274	5	Substrate binding By similarity
	Region	304 – 933	630	Formyltetrahydrofolate synthetase
Sites
	Binding site	195	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q27772-1 [UniParc]. Last modified January 16, 2004. Version 3. Checksum: 55C3FA820C1A55CB	FASTA	933	100,618
	10 20 30 40 50 60 MWEPQGSLDP VLESIENELR DQVAEARSRW AGFDARLAIV QVGGREDSNV YIRMKLRAAE 70 80 90 100 110 120 NIGITAEHIQ LPRDITETEL LANITSLNES PYVHGIIVQM PLDSVHPIDS HAITDAVSPD 130 140 150 160 170 180 KDVDGLNTIN EGRVRVGDLS GFIPCTPAGC VELIKRTGVT IAGKNVVVLG RSRIVGTPVS 190 200 210 220 230 240 ELLKWEHATV TVCHSKTKNL SEITKTADIL VVAIGRGEMV RGSWIKPGAV VIDCGINPIS 250 260 270 280 290 300 DPTKKSGQRL VGDVAYEEAV QVASHVTPVP GGVGPMTVAM LMRNTVQAAR RQLDRLLAPT 310 320 330 340 350 360 WPLRPLRITP LSPPPSDIVI ARSQKPKDIS ELAHEIGLFS NEVSQYGRTK AKISLSVLDR 370 380 390 400 410 420 MRNQQGAKYI VVAGITPTPL GEGKSTTLLG LVQALSAHRG RNSFAVMRQP SQGPTFGVKG 430 440 450 460 470 480 GAAGGGYSQV IPMEEFNLHL TGDIHAGTAA NNLLAAQMDA RIFHELTQKD GPLFDRLVPK 490 500 510 520 530 540 IKGVRKFSPI QLRRLKRLGI TKTDPDTLTE GEKSKFARLN IDTSKIMWNR VVDLNDRYLR 550 560 570 580 590 600 KITVGQSPTE KGFTRETAFD ISVASEIMAI LALGRDVEDI KERLANMVVA LDKSGNPVTA 610 620 630 640 650 660 DDLGMTGALL VLLRDAFEPT LMQSLEGTPV LVHTGPFANI RHGCSSILAD KIAMKLAGEN 670 680 690 700 710 720 GYVATEAGFG SDIGMEKFFD IKCRASGDTP HCAVIVSTVR ALKMHGGGPP VSAGMPLNDV 730 740 750 760 770 780 YVQENLELLS KGLCNLGKHI SNGNKFGVPV VVAINKHGND TPAELNLVKE FAVKNGAFRA 790 800 810 820 830 840 VLCDHWAKGG LGALELADAV IEACDSKSKF DFLYPLQLSI QEKIQIIAKE MYGAGQVEYT 850 860 870 880 890 900 DEVLEKIKTF TDMGYDKFPI CMAKTSNSLT GDPAVKGAPT GFTLKINGIF ASVGAGFVVP 910 920 930 MVGEISKMPG LPTRPSIYDI DLNTKTGEIE GLF

References

[1]	"Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda." Tremblay G.B., MacKenzie R.E. Biochim. Biophys. Acta 1261:129-133(1995) [PubMed: 7893749] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L36189 mRNA. Translation: AAA74302.1.
PIR	S53523.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.5. 15157. 3.5.4.9. 15157. 6.3.4.3. 15157.
Family and domain databases
InterPro	IPR000559. For_THF_ligase. IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01268. FTHFS. 1 hit. PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view]
PRINTS	PR00085. THFDHDRGNASE.
ProDom	PD002300. THFDhg/Cyc_hydro. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00721. FTHFS_1. 1 hit. PS00722. FTHFS_2. 1 hit. PS00766. THF_DHG_CYH_1. 1 hit. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C1TC_SPOFR

Accession

Primary (citable) accession number: Q27772

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	June 16, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)